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- PDB-1pan: A COMPARISON OF NMR SOLUTION STRUCTURES OF THE RECEPTOR BINDING D... -

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Entry
Database: PDB / ID: 1pan
TitleA COMPARISON OF NMR SOLUTION STRUCTURES OF THE RECEPTOR BINDING DOMAINS OF PSEUDOMONAS AERUGINOSA PILI STRAINS PAO, KB7, AND PAK: IMPLICATIONS FOR RECEPTOR BINDING AND SYNTHETIC VACCINE DESIGN
ComponentsPAO PILIN, TRANS
KeywordsFIMBRIAL PROTEIN
Function / homology
Function and homology information


type IV pilus / single-species biofilm formation on inanimate substrate / type IV pilus-dependent motility / cell adhesion involved in single-species biofilm formation / pilus / regulation of calcium-mediated signaling / host cell endoplasmic reticulum membrane / cell surface / plasma membrane / cytosol
Similarity search - Function
Fimbrial protein pilin / Pilin (bacterial filament) / : / Prokaryotic N-terminal methylation site. / Prokaryotic N-terminal methylation motif / Prokaryotic N-terminal methylation site / Pilin-like
Similarity search - Domain/homology
Type IV major pilin protein PilA
Similarity search - Component
Biological speciesPseudomonas aeruginosa (bacteria)
MethodSOLUTION NMR
AuthorsCampbell, A.P. / Mcinnes, C. / Hodges, R.S. / Sykes, B.D.
Citation
Journal: Biochemistry / Year: 1995
Title: Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7, and PAK: implications for receptor binding and synthetic vaccine design.
Authors: Campbell, A.P. / McInnes, C. / Hodges, R.S. / Sykes, B.D.
#1: Journal: Biopolymers / Year: 1994
Title: Conformational Differences between Cis and Trans Proline Isomers of a Peptide Antigen Representing the Receptor Binding Domain of Pseudomonas Aeruginosa as Studied by 1H NMR
Authors: Mcinnes, C. / Kay, C.M. / Hodges, R.S. / Sykes, B.D.
#2: Journal: Biochemistry / Year: 1993
Title: NMR Solution Structure and Flexibility of a Peptide Antigen Representing the Receptor Binding Domain of Pseudomonas Aeruginosa
Authors: Mcinnes, C. / Soennichsen, F.D. / Kay, C.M. / Hodges, R.S. / Sykes, B.D.
History
DepositionOct 5, 1995Processing site: BNL
Revision 1.0Jan 29, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf
Item: _pdbx_database_status.process_site
Revision 1.4Oct 30, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PAO PILIN, TRANS


Theoretical massNumber of molelcules
Total (without water)1,8711
Polymers1,8711
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
Representative

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Components

#1: Protein/peptide PAO PILIN, TRANS / FIMBRIAL PROTEIN


Mass: 1871.120 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Strain: O / References: UniProt: P04739
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other

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Processing

NMR softwareName: PEPFLEX II / Classification: refinement
NMR ensembleConformers submitted total number: 1

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